Recombinant antibodies

Laboratory animals are not used in the production of recombinant antibodies. The antibodies are produced exclusively in vitro. For this purpose, microorganisms are genetically transformed for example by introducing a DNA sequence encoding the antibody into the genome of the host cell. In many cases this involves only a part of the antibodies, or various conjugates in which the antibody fragment is coupled to another protein component (e.g., an enzyme or a pharmaceutical active substance). For various purposes, incomplete antibodies may be used. For many applications it is sensible to use only a part of the antibody. The proteolytic cleavage of an antibody produces several fragments, which are often mentioned in association with antibodies (Fig. 1).

Figure 1: Proteolytic digestion of an antibody with papain and pepsin. In the first case the antibody is split above the hinge region, thereby producing a so-called Fc fragment (consisting of two heavy-chain constant domains) and two Fab fragments (variable and constant domain of the two chains). On cleavage with pepsin, the cut is made below the hinge. The two Fab fragments are linked (F(ab´)2) and the Fc fragment is cleaved into multiple segments, the largest of which is designated pFc’.

The antibody fragments retain their properties after cleavage. Fab and F(ab’)2 continue to bind their antigen specifically, but due to the lack of Fc fragment they have no effect on cells that have Fc receptors. Due to their small size, the fragments are well suited for therapeutic purposes because they can reach their application sites more easily. The Fc fragment also maintains its function and can be used, for example, to block the cells’ Fc receptors.

We offer the following recombinant antibodies:

On antibodies-online you can find some well selected recombinant antibodies. Click on the links to find product details.